Saliva and Serum Protein Adsorption on Chemically Modified Silica Surfaces.

Saliva and Serum Protein Adsorption on Chemically Modified Silica Surfaces.
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唾液和血清蛋白在化学改性二氧化硅表面上的吸附。

DOI:
10.1177/00220345211022273
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发表时间:
2021-09
影响因子:
7.6
通讯作者:
Ruhl S
Ruhl S
中科院分区:
医学1区
文献类型:
--
作者:
Lehnfeld J;Dukashin Y;Mark J;White GD;Wu S;Katzur V;Müller R;Ruhl S

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生物材料一旦插入口腔,立即被一层吸附蛋白覆盖,该蛋白主要由唾液蛋白组成,但如果生物材料靠近牙龈缘放置或如果其植入组织和骨中,则也由血浆蛋白组成。通常是这种蛋白质层,而不是原始的生物材料表面,随后被定植的细菌或附着的组织细胞遇到。因此,研究这一重要的初始蛋白质吸附从人的唾液和血清,以及它如何可能受到影响,通过化学改性的生物材料表面,我们已经测量了蛋白质的吸附量,并分析了吸附的蛋白质层的组成,使用凝胶电泳和蛋白质印迹。在这里,我们开发了一个基于二氧化硅表面的体外模型系统,用7种基于硅烷的自组装单分子层进行化学修饰,这些单分子层跨越了从亲水到疏水表面的广泛的物理化学性质(水接触角从15°到115°),表面自由能从低到高(12至57 mN/m),和负至正表面电荷(在生理pH下ζ电位为-120至+40 mV)。我们发现,化学表面功能产生了重大影响的蛋白质吸附的总量,但是,没有观察到的物理化学表面参数的吸附量的线性相关性。只有几个单一的蛋白质组分的吸附行为,从物理化学数据,似乎遵循物理化学的预期。例如血清中的白蛋白和唾液中的溶菌酶;在这两种情况下,吸附都有利于带反电荷的表面。从这些发现中,我们得出结论,在复杂的生物流体,如唾液和血清,吸附行为是由表面的整体蛋白质结合能力,而不是由特定的物理化学相互作用的单一蛋白质实体的表面占主导地位。
Biomaterials, once inserted in the oral cavity, become immediately covered by a layer of adsorbed proteins that consists mostly of salivary proteins but also of plasma proteins if the biomaterial is placed close to the gingival margin or if it becomes implanted into tissue and bone. It is often this protein layer, rather than the pristine biomaterial surface, that is subsequently encountered by colonizing bacteria or attaching tissue cells. Thus, to study this important initial protein adsorption from human saliva and serum and how it might be influenced through chemical modification of the biomaterial surface, we have measured the amount of protein adsorbed and analyzed the composition of the adsorbed protein layer using gel electrophoresis and western blotting. Here, we have developed an in vitro model system based on silica surfaces, chemically modified with 7 silane-based self-assembled monolayers that span a broad range of physicochemical properties, from hydrophilic to hydrophobic surfaces (water contact angles from 15° to 115°), low to high surface free energy (12 to 57 mN/m), and negative to positive surface charge (zeta potentials from –120 to +40 mV at physiologic pH). We found that the chemical surface functionalities exerted a substantial effect on the total amounts of proteins adsorbed; however, no linear correlation of the adsorbed amounts with the physicochemical surface parameters was observed. Only the adsorption behavior of a few singular protein components, from which physicochemical data are available, seems to follow physicochemical expectations. Examples are albumin in serum and lysozyme in saliva; in both, adsorption was favored on countercharged surfaces. We conclude from these findings that in complex biofluids such as saliva and serum, adsorption behavior is dominated by the overall protein-binding capacity of the surface rather than by specific physicochemical interactions of single protein entities with the surface.
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